PleD allosteric product inhibition

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Allosteric product inhibition


PleD shows direct non-competitive feedback inibition with a Ki of about 1 μM. There are two allosteric sites, the primary inhibition site Ip (R359 and D362 of a RxxD sequence motif and R390), and the "secondary'' inhibition site Is (R313) in the PleD GGDEF domain that are involved in product  binding across to GGDEF domains (cross-linking).

Binding of two intercalated (c-di-GMP)2 dimers results in cross-linking of the two GGDEF domains in the dimer and keeps the two active sites (with bound substrate analog ) apart form each other.